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PDBsum entry 4ag2

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protein ligands metals Protein-protein interface(s) links
Hydrolase/de novo protein PDB id
4ag2

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
223 a.a.
58 a.a.
Ligands
MES ×2
LMR ×3
Metals
_NA ×5
Waters ×514
PDB id:
4ag2
Name: Hydrolase/de novo protein
Title: Human chymase - fynomer complex
Structure: Chymase. Chain: a, b. Synonym: alpha-chymase, mast cell protease i. Engineered: yes. Fynomer. Chain: c, d. Engineered: yes
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic construct. Organism_taxid: 32630. Expression_system_taxid: 562
Resolution:
1.80Å     R-factor:   0.180     R-free:   0.212
Authors: D.Schlatter,S.Brack,D.W.Banner,S.Batey,J.Benz,J.Bertschinger,W.Huber, C.Joseph,A.Rufer,A.Van Der Kloosters,M.Weber,D.Grabulovski,M.Hennig
Key ref: D.Schlatter et al. (2012). Generation, characterization and structural data of chymase binding proteins based on the human Fyn kinase SH3 domain. Mabs, 4, 497-508. PubMed id: 22653218
Date:
23-Jan-12     Release date:   11-Jul-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P23946  (CMA1_HUMAN) -  Chymase from Homo sapiens
Seq:
Struc:
247 a.a.
223 a.a.
Protein chains
No UniProt id for this chain
Struc: 58 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.3.4.21.39  - chymase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.

 

 
Mabs 4:497-508 (2012)
PubMed id: 22653218  
 
 
Generation, characterization and structural data of chymase binding proteins based on the human Fyn kinase SH3 domain.
D.Schlatter, S.Brack, D.W.Banner, S.Batey, J.Benz, J.Bertschinger, W.Huber, C.Joseph, A.Rufer, A.van der Klooster, M.Weber, D.Grabulovski, M.Hennig.
 
  ABSTRACT  
 
No abstract given.

 

 

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